VAMP1
Function
Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Involvement in disease
Spastic ataxia 1, autosomal dominant
SPAX1
An autosomal dominant form of spastic ataxia, a progressive neurodegenerative disorder characterized by lower-limb spasticity and generalized ataxia with dysarthria, impaired ocular movements, and gait disturbance.
None
The disease is caused by variants affecting the gene represented in this entry. A mutation affecting a critical donor site for the splicing of VAMP1 isoforms leads to the loss of neuron-specific isoform 1 and subsequently results in haploinsufficiency (PubMed:22958904). Therefore, there would be less neurotransmitter exocytosis in specific regions of the brain, causing the symptoms of SPAX1.
Myasthenic syndrome, congenital, 25, presynaptic
CMS25
A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features include easy fatigability and muscle weakness. CMS25 is an autosomal recessive form characterized by hypotonia and generalized muscle weakness apparent from birth. Affected individuals have feeding difficulties and delayed motor development, usually never achieving independent ambulation. Additional variable features include eye movement abnormalities, joint contractures, and rigid spine.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which probably hydrolyzes the 78-Gln-|-Phe-79 bond and inhibits neurotransmitter release (PubMed:22289120).
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which probably hydrolyzes the 61-Arg-|-Leu-62 bond and inhibits neurotransmitter release (PubMed:22289120). BoNT/D has low catalytic activity on this protein due to its sequence (PubMed:22289120). Note that humans are not known to be infected by C.botulinum type D.
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type F (BoNT/F, botF) which probably hydrolyzes the 60-Gln-|-Lys-61 bond and inhibits neurotransmitter release (PubMed:22289120).
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which probably hydrolyzes the 68-Arg-|-Ala-69 bond and inhibits neurotransmitter release (PubMed:29540745). It remains unknown whether BoNT/X is ever produced, or what organisms it targets.
Sequence Similarities
Belongs to the synaptobrevin family.
Tissue Specificity
Nervous system, skeletal muscle and adipose tissue.
Cellular localization
- Isoform 1
- Cytoplasmic vesicle
- Secretory vesicle
- Synaptic vesicle membrane
- Single-pass type IV membrane protein
- Synapse
- Synaptosome
- Isoform 2
- Cytoplasmic vesicle membrane
- Single-pass type IV membrane protein
- Synapse
- Synaptosome
- Isoform 3
- Mitochondrion outer membrane
- Single-pass type IV membrane protein
Alternative names
SYB1, VAMP1, Vesicle-associated membrane protein 1, VAMP-1, Synaptobrevin-1